The partial purification and properties of pepsin obtained from Turkey proventriculus

Temiz H., Aykut U., Okumus E., Turhan S.

BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, vol.12, no.4, pp.450-456, 2007 (SCI-Expanded) identifier

  • Publication Type: Article / Article
  • Volume: 12 Issue: 4
  • Publication Date: 2007
  • Doi Number: 10.1007/bf02931070
  • Journal Name: BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.450-456
  • Keywords: enzyme purification, Turkey proventriculus, pepsin, proteolytic activity, gel filtration, MILK-CLOTTING ENZYME, CYNARA-CARDUNCULUS, CHICKEN PEPSIN, PROTEASES, TEMPERATURE, EXTRACTS, PH
  • Ondokuz Mayıs University Affiliated: Yes

Abstract

In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1:2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SIDS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results. (c) KSBB.